Black M E, Hruby D E
Department for Microbiology, Oregon State University, Corvallis 97331-3804.
Biochem Biophys Res Commun. 1990 Jun 29;169(3):1080-6. doi: 10.1016/0006-291x(90)92005-k.
Thymidine kinase enzymes isolated from a variety of sources are generally considered to have a native molecular weight of 80-90 kDa composed of two 40-45 kDa subunits. Although these parameters may accurately describe the atypical deoxypyrimidine kinases expressed by members of the Herpesviridae, the nucleotide sequences of thymidine kinase genes isolated from human, mouse, chicken and variety of poxviruses (vaccinia virus, monkeypox virus, variola virus, fowlpox virus and capripoxvirus) predict molecular weights on the order of 20-25 kDa for the derived primary translation products. To resolve this apparent dilemma, velocity sedimentation centrifugation, gel filtration chromatography and protein cross-linking procedures were employed to provide experimental evidence that enzymatically-active vaccinia virus thymidine kinase is a homotetrameric complex of 20 kDa monomers with a native Mr of 80 kDa.
从多种来源分离得到的胸苷激酶通常被认为其天然分子量为80 - 90 kDa，由两个40 - 45 kDa的亚基组成。尽管这些参数可能准确描述了疱疹病毒科成员所表达的非典型脱氧嘧啶激酶，但从人、小鼠、鸡以及多种痘病毒（痘苗病毒、猴痘病毒、天花病毒、禽痘病毒和山羊痘病毒）中分离得到的胸苷激酶基因的核苷酸序列预测，其推导的初级翻译产物的分子量约为20 - 25 kDa。为了解决这一明显的困境，采用了速度沉降离心、凝胶过滤色谱和蛋白质交联程序，以提供实验证据表明具有酶活性的痘苗病毒胸苷激酶是一种由20 kDa单体组成的同四聚体复合物，其天然分子量为80 kDa。
